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A3PF79 (PUR5_PROM0) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoribosylformylglycinamidine cyclo-ligase

EC=6.3.3.1
Alternative name(s):
AIR synthase
AIRS
Phosphoribosyl-aminoimidazole synthetase
Gene names
Name:purM
Ordered Locus Names:P9301_17811
OrganismProchlorococcus marinus (strain MIT 9301) [Complete proteome] [HAMAP]
Taxonomic identifier167546 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole. HAMAP-Rule MF_00741

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2. HAMAP-Rule MF_00741

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00741.

Sequence similarities

Belongs to the AIR synthase family.

Ontologies

Keywords
   Biological processPurine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_process'de novo' IMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoribosylformylglycinamidine cyclo-ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 347347Phosphoribosylformylglycinamidine cyclo-ligase HAMAP-Rule MF_00741
PRO_1000046453

Sequences

Sequence LengthMass (Da)Tools
A3PF79 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 34E38E2002A248FD

FASTA34738,537
        10         20         30         40         50         60 
MDYKTSGVDI EAGREFVSEI KQAVEATHTS NVIEGIGGFG GLFRIPIDSF KKPVLVSGTD 

        70         80         90        100        110        120 
GVGTKLELAQ SKNFHFEVGI DLVAMCMNDI ITSGARPLFF LDYIATGKLD KKQLLRVVQG 

       130        140        150        160        170        180 
ISHGCGENNC SLLGGETAEM PGFYSKNKYD LAGFCVGIVD EDKLINGKKV SENDLIIALK 

       190        200        210        220        230        240 
SNGVHSNGFS LVRKIIQNNN QIDKEFEKVS HLNFYDELLK PTKIYNNVIN QMLSEDIEIK 

       250        260        270        280        290        300 
AMSHITGGGI PENLPRCIPS DFIPYINTSS WQIPTLFKFL KEKGSIPERD FWNTFNLGVG 

       310        320        330        340 
FCLIIDKQFK DAILSICKDY GIDSWEIGKI VRKNDSTISK FLPEILT 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9301.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000576 Genomic DNA. Translation: ABO18404.1.
RefSeqYP_001092005.1. NC_009091.1.

3D structure databases

ProteinModelPortalA3PF79.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167546.P9301_17811.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO18404; ABO18404; P9301_17811.
GeneID4911847.
KEGGpmg:P9301_17811.
PATRIC22997071. VBIProMar103344_1705.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0150.
HOGENOMHOG000229090.
KOK01933.
OMAHCVNDIL.
OrthoDBEOG61CM1V.
ProtClustDBPRK05385.

Enzyme and pathway databases

BioCycPMAR167546:GH1Y-1830-MONOMER.
UniPathwayUPA00074; UER00129.

Family and domain databases

Gene3D3.30.1330.10. 1 hit.
3.90.650.10. 1 hit.
HAMAPMF_00741_B. AIRS_B.
InterProIPR010918. AIR_synth_C_dom.
IPR000728. AIR_synth_N_dom.
IPR004733. PurM_cligase.
IPR016188. PurM_N-like.
[Graphical view]
PfamPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 1 hit.
[Graphical view]
SUPFAMSSF55326. SSF55326. 1 hit.
SSF56042. SSF56042. 1 hit.
TIGRFAMsTIGR00878. purM. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR5_PROM0
AccessionPrimary (citable) accession number: A3PF79
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 3, 2007
Last modified: April 16, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways